ID A0A8V0XIV7_CHICK Unreviewed; 3155 AA.
AC A0A8V0XIV7;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=Laminin subunit alpha 3 {ECO:0000313|Ensembl:ENSGALP00010006626.1};
GN Name=LAMA3 {ECO:0000313|Ensembl:ENSGALP00010006626.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010006626.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010006626.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Broiler {ECO:0000313|Ensembl:ENSGALP00010006626.1};
RA Warren W., Formenti G., Fedrigo O., Haase B., Mountcastle J., Balacco J.,
RA Tracey A., Schneider V., Okimoto R., Cheng H., Hawken R., Howe K.,
RA Jarvis E.D.;
RT "Gallus gallus (Chicken) genome, bGalGal1, GRCg7b, maternal haplotype
RT autosomes + Z & W.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGALP00010006626.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010006626.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGALP00010006626.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010006626.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR FunCoup; A0A8V0XIV7; 145.
DR GlyGen; A0A8V0XIV7; 2 sites.
DR Ensembl; ENSGALT00010011819.1; ENSGALP00010006626.1; ENSGALG00010004966.1.
DR GeneTree; ENSGT00940000155638; -.
DR OrthoDB; 18487at2759; -.
DR Proteomes; UP000000539; Chromosome 2.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA.
DR GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 14.
DR CDD; cd00110; LamG; 4.
DR FunFam; 2.10.25.10:FF:000011; Cadherin EGF LAG seven-pass G-type receptor; 1.
DR FunFam; 2.10.25.10:FF:000083; Laminin subunit alpha; 2.
DR FunFam; 2.10.25.10:FF:000090; laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000388; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000069; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000033; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000084; Laminin subunit alpha 3; 1.
DR FunFam; 2.60.120.200:FF:000056; Laminin subunit alpha 3; 1.
DR FunFam; 2.10.25.10:FF:000209; Laminin subunit alpha 5; 1.
DR FunFam; 2.60.120.200:FF:000150; Laminin subunit alpha 5; 1.
DR FunFam; 2.60.120.260:FF:000022; Laminin subunit alpha 5; 1.
DR FunFam; 2.10.25.10:FF:000188; Laminin subunit gamma 2; 1.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 12.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR050440; Laminin/Netrin_ECM.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF.
DR PANTHER; PTHR10574:SF445; LAMININ SUBUNIT ALPHA 3; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; EGF_laminin; 12.
DR Pfam; PF24973; EGF_LMN_ATRN; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 14.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 4.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 8.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}; Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8V0XIV7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2701..2725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2772..2791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..304
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 497..541
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 542..594
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 637..689
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1215..1260
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1305..1353
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1354..1404
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1425..1604
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1638..1684
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1685..1737
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2806..2988
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2986..3152
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1791..1859
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1905..2000
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2035..2103
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2245..2289
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 497..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 517..526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 542..554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 544..561
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 563..572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 660..669
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1215..1227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1217..1234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1236..1245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1329..1338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1354..1366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1356..1373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1375..1384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1657..1666
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1685..1697
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1708..1717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3155 AA; 350820 MW; BD276F66E1E24A87 CRC64;
HFLPGSSAHP AAASPQRGCV RASPPPGCRL LWALLPPLFS LCPAQTEPPG SLGLSLHPPY
FNLAETAGIS ATATCGEEEG GGRPELYCKL VGGPAAAPLG RAIQGQFCDY CNAGDPSKAH
PITNAIDGTE RWWQSPPLSK GLKYNEVNVT LDLGQLFHVA YILIKFANSP RPDLWILERS
VDFGRTYTPW QYFAHSKADC LERFGKEANV PVRRDSDVIC TTEYSRIVPL ENGEIVVSLV
NGRPGAKNFT YSPGLREFTK ATNIRLHFLR TNTLLGHLIS KAQRDPTVTR RYYYSIKDIS
IGGRCVCHGH AEVCNAKSAE NQYQFHCECQ HNTCGETCDH CCPGYNQKQW QPLTWSIAFP
ACNCHGHATD CYYDADVDQR RESLNIHGHY EGGGVCINCQ HNTAGVNCEK CAKGYYRPYG
VPARAPDGCI SCPCDLERAE GCEEGSGRCF CKWNFQGENC EHCADGFYSF PFCIHIPVYP
FTSPNPRDAI AGDITVCECN SVGTQPEVCD FLGRCLCRSG VVGLQCDSCQ PGHHSFPICE
ACQCSPLGSR HSICEPTTGQ CECQTNVTGR QCDRCISAAP SFPYCEGINS ECNPSGSIDS
HSGYCQCLQH VEGPTCSKCK PLYWNLAEEN PEGCTACQCD VSGTLSGVGE CQQETGRCYC
KSNVCGDFCN TCEAGYYALE NKNYFGCKGC QCDVGGSISF ACAEPSGACQ CREHVVGKAC
QEPEKNYFFP DLHHMKFEIE DGTTVKGKEI RFGYDPEEFP SFSWRGYARM SSIQNEVRIT
LNVEKSNLYL FRIILRYINP GGESLSGRIS ACAAQSKEFV FPPSKEPAFV TIPGKNSTEP
FSLVSGAWTV SIVAEDVLLD YMVLLPRDYY EASILQIQVT EPCTYSGHVS TENCLLYQHL
PLGKFSCVLA SEAVYFRHGV KHGIPVRQPS PGQPVMSHIS GREVNLQMTI NVPHVGRYVL
VFEYTNEDDQ LYTAEVTVNS PGPVTEGRVR IYSCKYSFLC RSVVVDDRNR IAAYDLLADT
KIHLQASSIN FLLEICSKVH KNKNISQKNV LPELLLFLQN QVTMTGRVPR LGKYVFVVHF
YQPAYPTFPV VLAHWSLFGI ILLGSFNASF CPHSSGCRDQ VIAENQIELD ISEPEVSVTV
MIPDRRMLVL ESVLVVPADS YSFKILDKKT VDKSFDFITQ CGGNSFHIDP ERSSAFCKDS
ARSLVAFYNN GAVPCNCHSE GSMSPTCSPL GGQCICRPNV IGRQCSRCQT GYYGFPSCKL
CNCGQRLCDD LTGKCICPPR TVKPKCEVCE RYYFSYHPLA GCESCNCSER GVVNAARPEC
EKNNGQCKCK PGIRGRQCDR CAPGTYDFPN CIPCKCNRDG TEPDVCDPQT GICLCKENVE
GAECDICRPG SFYLDPSNPK GCTTCFCFGV TSSCRSTNRR RTKFVDMRNW RLEAMDENID
IPVTFNPVSN SVVADVQELP ASVHSLYWKA PPSYLGEKLS SYGGFLSYQV KSFGLPSEGM
VLLDKKPEII LTGQQMKIVY VDPNNPLPDR QYYGRVQLVE GNFRHASSNN HVSREELMVI
LSRLDALHIR GLYFTETQRL TLGEVGLEET TSTGSGSIAY NVETCSCPPE YAGDSCQDCG
LGFYRESKGL FSGRCVPCNC NGNSNRCHDG TGKCINCQYN TAGEKCELCK DGYFGDATQG
SCRICPCPYT NRFATGCVAN GEEIQCLCKE GYTGVRCERC APGYFGNPQK YGGYCQKCNC
NNNGQLASCD RLTGECFNNE PKDVDPNEDC DSCDSCVITL LKDLSTIGDE LQLIKSQLQN
VRADANTLEQ MRQLEIRIKD LKVLLNNYRS VLHNQGSKAD ELEKEFSKLN HDLNALQEKV
ETSPSFESSA WCVLCLNLTF FFFFLNPVLL EQIAGTNSEV NNLPLGDAAK ELAEAQRMMR
EMRNRNFGQL QTDAEKERTE ARLLLARVKN ELQKYHQENH GLVKIMRDSL NEYESKLTDL
REALNEATGQ TKQAENLNRE NGVLLADIKV MLGILDILSS AQSSLTQANS MLGLLQKSKE
EYESLSAQLD GARKDMNGKL TNSSLSASKE PLVVRAEEHA KSLQDLAKQL EEIKNNARKD
ELVGCAVEAS TAYDDIINAI KAAEEAANKA GSAADSALSG LHCFAAIGPT LEDIKQRLGV
TDGKKNTLQI DLVTLQNNLN GINRDDIDDI ITSAKNMVKS AKDVTTNVLD ELLPIQEDVE
KMKGTYGSTQ SAGFNKALTE ANNSVKKLTN QLPDLFSKIE SINQQLMPIS NISENVNRIR
ELIQRAREAA NKVAIPMRFN GSSGVEVRPP SNLEDLKAYT SLTFFLQRPQ KRLDVPQRAS
NKFVLYLGNK DASKGYIGMA VKDGHLTCVY NLGDREAEVV VDPLVMQSNT EEAIMDQVKL
ERIYQYVKLN YIKAATSASP VFEKPLTASS GDGNTLLNLD PSTVVFYVGG YPPDFRPPRK
LDYPHYEGCI ELDNLNENVK VRYRCRENDE SDQSYFEGTG YASVTSKETN ANTRIRYEQT
IQTTADEGIV FFAANEDQYI SVLIKNGHPV FRYKIDSELP KEIENNVTLN DGTHKQVSHF
KQLNDRCFRL LNSFFLPLPE TSFDITVPPF RGCMKNVKTP ETASVVFDET VGVSKKCSDD
WKLVRSAAFS KKGTLSLSAA SFPFPRDFQV GFGFRTMAST GTLLSYNLWK THQSNVSFLN
IYFIQIHGCI SLDFMLVFLC FFFFFRVRLL VDDDPDTKSF DFLRSQTFIQ PIRFGGDDFE
GCISNVFIER YLAWWTFSFI HFCLLQLSFT FRRQALQNTA IPPKMSSAFH KLSFTGAFLE
NRENTTPDKI DVCLNMLTFH YRLHFSVDIR TRSSRGLIVF MEGRSENSYT ALHISKGRFV
FSLGSGRRRI KIKTSVKYND GQWHTVVCSR DGENVLLVVD GLRAQHGRLG RLGRASTNDI
KPPVYLGGPP LLKRQNIPMK SFKGCLRNFK MNGKVMNTPQ QKKDVLPCLD APMEMGIHFF
KEGGYVAVGK IVFAIRPRRS TGVLLHSGSK PDNYLTIYMK EGKVRTGCNS ITAVLPSFKL
SFTCFFAVSQ KVNTLQLEVG TESNYTTGHP PFSPEYVHQP LYFGKIPENL DSQWLPVKDP
FFGCLWNISI DGKPVSTKKI SEVHGAVSLR GCPAT
//
